gag Antibody

1. Taken together, the authors interpret these results to mean that Gag membrane interaction is cooperative in that it depends on the ability of Gag to multimerize. PMID: 26676779
2. The resulting model of the RSV Gag lattice shows features and dynamics of the capsid protein with implications for the maturation process, and confirms the stabilizing role of the upstream and downstream regions of Gag, namely p10 and SP-NC. PMID: 26118533
3. The structure of immature virus-like Rous sarcoma virus Gag particles reveals a structural role for the p10 domain in assembly. PMID: 26223638
4. RSV Gag is highly flexible and can adopt a folded-over conformation on a lipid bilayer, implicating both the N and C termini in membrane binding. PMID: 26246573
5. Taken together, these results provide strong evidence for the formation of a critical six-helix bundle in Gag assembly. PMID: 24599998
6. These data suggest a possible connection between Gag nuclear trafficking and phosphoinositide-dependent plasma membrane targeting. PMID: 23325682
7. Taken together, the authors interpret these results to mean that Rous sarcoma virus Gag membrane association is driven by electrostatic interactions and not by any specific association with phosphatidylinositol-(4,5)-bisphosphate. PMID: 21813603
8. Directionality of nucleocytoplasmic transport of the retroviral gag protein depends on sequential binding of karyopherins and viral RNA. PMID: 20435918
9. The authors conclude that the wild-type capsid protein sequence represents an evolutionary compromise between competing requirements for optimization of Gag assembly (of the immature virion) and capsid assembly (in the maturing virion). PMID: 20427531
10. These data support a model in which the gag protein LYPSL motif of Rous sarcoma virus mediates budding through an interaction with the ESCRT adaptor protein Alix. PMID: 20392845
11. ubiquitination of Gag is dependent upon Nedd4 binding to the L domain during RSV budding pathway PMID: 15564502
12. the nucleocytoplasmic dynamics of RSV Gag depend upon the counterbalance of Crm1p-mediated export with two independent NLSs, each interacting with distinct nuclear import factors. PMID: 16439536
13. These results indicate that the p10 NES domain of Gag is critical for virus replication and that it plays overlapping roles required for the nuclear shuttling of Gag and for the maintenance of proper virion core morphology. PMID: 17634229
14. these experimental results strongly suggest that Rous sarcoma virus Gag proteins are capable of interacting within the nucleus. PMID: 17977961
15. These findings provide important biological evidence in support of a significant conformational change involving the dimerization helix and the major homology region during capsid protein maturation. PMID: 18433823
16. Taken together, these results define a short assembly domain between the folded portions of CA and NC, which is essential for formation of the immature Gag shell. PMID: 18448521
17. cryo-electron microscopic analyses of two in-vitro-assembled capsids of Rous sarcoma virus PMID: 19194444
18. Inserting a bipartite nuclear localization signal into Gag enhanced nuclear localization and restored RNA packaging in mutant viruses. PMID: 19369339

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KEGG: vg:1491923